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dc.contributor.author
Barrantes, Francisco Jose
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Antollini, Silvia Susana
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Blanton, Michael P.
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Prieto, Manuel
dc.date.available
2019-03-15T19:51:50Z
dc.date.issued
2000-12
dc.identifier.citation
Barrantes, Francisco Jose; Antollini, Silvia Susana; Blanton, Michael P.; Prieto, Manuel; Topography of nicotinic acetylcholine receptor membrane-embedded domains; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 275; 48; 12-2000; 37333-37339
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/71787
dc.description.abstract
The topography of nicotinic acetylcholine receptor (AChR) membrane-embedded domains and the relative affinity of lipids for these protein regions were studied using fluorescence methods. Intact Torpedo californica AChR protein and transmembrane peptides were derivatized with N-(1-pyrenyl)maleimide (PM), purified, and reconstituted into asolectin liposomes. Fluorescence mapped to proteolytic fragments consistent with PM labeling of cysteine residues in αM1, αM4, γM1, and γM4. The topography of the pyrene-labeled Cys residues with respect to the membrane and the apparent affinity for representative lipids were determined by differential fluorescence quenching with spin-labeled derivatives of fatty acids, phosphatidylcholine, and the steroids cholestane and androstane. Different spin label lipid analogs exhibit different selectivity for the whole AChR protein and its transmembrane domains. In all cases labeled residues were found to lie in a shallow position. For M4 segments, this is compatible with a linear α-helical structure, but not so for M1, for which 'classical' models locate Cys residues at the center of the hydrophobic stretch. The transmembrane topography of M1 can be rationalized on the basis of the presence of a substantial amount of non-helical structure, and/or of kinks attributable to the occurrence of the evolutionarily conserved proline residues. The latter is a striking feature of M1 in the AChR and all members of the rapid ligand-gated ion channel superfamily.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Nicotinic Acetylcholine Receptor
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Lipids
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Ion Channel
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Topography of nicotinic acetylcholine receptor membrane-embedded domains
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-14T14:18:31Z
dc.journal.volume
275
dc.journal.number
48
dc.journal.pagination
37333-37339
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Barrantes, Francisco Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
dc.description.fil
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
dc.description.fil
Fil: Blanton, Michael P.. Texas Tech University; Estados Unidos
dc.description.fil
Fil: Prieto, Manuel. Universidade de Lisboa; Portugal
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M005246200
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/275/48/37333
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